ID A0A3B4URV5_SERDU Unreviewed; 910 AA.
AC A0A3B4URV5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Dystroglycan 1 {ECO:0000256|ARBA:ARBA00026224};
DE AltName: Full=Dystroglycan {ECO:0000256|ARBA:ARBA00031034};
DE AltName: Full=Dystrophin-associated glycoprotein 1 {ECO:0000256|ARBA:ARBA00030092};
GN Name=DAG1 {ECO:0000313|Ensembl:ENSSDUP00000021386.1};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000021386.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000021386.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: The dystroglycan complex is involved in a number of processes
CC including laminin and basement membrane assembly, sarcolemmal
CC stability, cell survival, peripheral nerve myelination, nodal
CC structure, cell migration, and epithelial polarization.
CC {ECO:0000256|ARBA:ARBA00023567}.
CC -!- FUNCTION: Transmembrane protein that plays important roles in
CC connecting the extracellular matrix to the cytoskeleton. Acts as a cell
CC adhesion receptor in both muscle and non-muscle tissues. Receptor for
CC both DMD and UTRN and, through these interactions, scaffolds axin to
CC the cytoskeleton. Also functions in cell adhesion-mediated signaling
CC and implicated in cell polarity. {ECO:0000256|ARBA:ARBA00024991}.
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC {ECO:0000256|ARBA:ARBA00004135}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004251}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}. Nucleus, nucleoplasm
CC {ECO:0000256|ARBA:ARBA00004642}. Postsynaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034100}. Secreted, extracellular space
CC {ECO:0000256|ARBA:ARBA00004239}. Synaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034109}.
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DR AlphaFoldDB; A0A3B4URV5; -.
DR STRING; 41447.ENSSDUP00000021386; -.
DR Ensembl; ENSSDUT00000021779.1; ENSSDUP00000021386.1; ENSSDUG00000015565.1.
DR GeneTree; ENSGT00390000008429; -.
DR OMA; FQLKVPP; -.
DR OrthoDB; 3598963at2759; -.
DR Proteomes; UP000261420; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IEA:InterPro.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd11305; alpha_DG_C; 1.
DR CDD; cd11303; Dystroglycan_repeat; 1.
DR Gene3D; 3.30.70.1040; Dystroglycan, domain 2; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR027468; Alpha-dystroglycan_domain_2.
DR InterPro; IPR041631; Alpha_DG1_N2.
DR InterPro; IPR006644; Cadg.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR008465; DAG1_C.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR030398; SEA_DG_dom.
DR PANTHER; PTHR21559:SF22; DYSTROGLYCAN 1; 1.
DR PANTHER; PTHR21559; DYSTROGLYCAN-RELATED; 1.
DR Pfam; PF18424; a_DG1_N2; 1.
DR Pfam; PF05454; DAG1; 1.
DR SMART; SM00736; CADG; 2.
DR SUPFAM; SSF49313; Cadherin-like; 2.
DR SUPFAM; SSF111006; Dystroglycan, domain 2; 1.
DR PROSITE; PS51699; SEA_DG; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 764..790
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 621..730
FT /note="Peptidase S72"
FT /evidence="ECO:0000259|PROSITE:PS51699"
FT REGION 92..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..381
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..888
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 910 AA; 99514 MW; 960FA93067BC4B0F CRC64;
MWPPQLFIDI CWAPQRPIAM HYKRRDMSCG DAGRSRLLSC RTIPLVIGLL VTMAPGTVPE
QQETLVEMIS VELEASMQSS VLSELQAAAS SVGEGPPTAI PDSSTKNRGV HTGIPDSSAI
VGQVFQLKVP PGPANASCNI HLTEMGKETL PSWLYWDKES CILRGLALDQ DKGVYHILVS
GEELIEKTGS QLSPSTVFSI EVYPEERADS EPALLTLQSD ISGLQPFTCG SEEPVTVLTV
ILDADLTKMV AEQRANLLGI MRKFSHVPLE QMRVVPVVNN RLFDMSAFMA GPGNAKKVVE
NGALLSWKLG CALDQGSIPD ISSVQSSAKD GNMSARLGYP VVGWHIVNKK PHGVKRVRRQ
LNNTPTPVPS LLPPTTHPEP PIRVVPTPTS PSIAPATDNS APPVRGPLPL PVKPTMRVRD
QIAHTPVFGP PQPTRVLGTT STIPIQPTMT RPTFVEATAV PTPPSTTKRP KTSATRKPKK
PKSSTPAPRE PKSTTAKPPR RTTPLSLAPD LNQTPEMRNP IDQVNAWVGT YFEVKIPPDT
FYDREDGTTD KLRLTLKKTP KEAVNETSWI QFNSTIQLLY GLPEEHHAGK HEYFMLATDK
GGRSIMDAFE VRVNRWSIND KPSVVFAARF HGDPKTLSND VHKKILLTKK LAYALGDRNS
STVTLRSITR GSIVVEWTNN SLQQSPCPKD QITVLSNRIS DPQGTPKLAF IKAMEPEFKP
INISIRGTNK CQSYTFIPPG EVPSPVLPTA TPSPGTGRRS SDDVYLHTVI PAVVVAALLL
IAGIIAMVCY RKKRKGKMTI EEQATFIKKG VPIIFADELD DSKSPPSSSI PLILQEEKPP
LPPPEYPNMA GPHSTLLNQD LLEEYSVYQD DDPNAPPYQP PPPFTVPIEG KGSRPKNMTA
YRSPPPYVPP
//
